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P04896 (GNAS2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Alternative name(s):
Adenylate cyclase-stimulating G alpha protein
Gene names
Name:GNAS
Synonyms:GNAS1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. Stimulates the Ras signaling pathway via RAPGEF2 By similarity.

Subunit structure

G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts with CRY1; the interaction may block GPCR-mediated regulation of cAMP concentrations.

Subcellular location

Cell membrane; Lipid-anchor By similarity.

Miscellaneous

The GNAS locus is imprinted in a complex manner, giving rise to distinct paternally, maternally and biallelically expressed proteins.

Sequence similarities

Belongs to the G-alpha family. G(s) subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransducer
   PTMIsopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-activating adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

adenylate cyclase-activating dopamine receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cartilage development

Inferred from electronic annotation. Source: Ensembl

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hindlimb morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Inferred from electronic annotation. Source: Ensembl

genetic imprinting

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

post-embryonic body morphogenesis

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sensory perception of chemical stimulus

Inferred from Biological aspect of Ancestor. Source: RefGenome

skin development

Inferred from electronic annotation. Source: Ensembl

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

extrinsic component of cytoplasmic side of plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionG-protein beta/gamma-subunit complex binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ionotropic glutamate receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mu-type opioid receptor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Gnas-1 (identifier: P04896-1)

Also known as: Alpha-S2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Gnas-2 (identifier: P04896-2)

Also known as: Alpha-S1;

The sequence of this isoform differs from the canonical sequence as follows:
     71-84: Missing.
Isoform Nesp55 (identifier: O18979-1)

The sequence of this isoform can be found in the external entry O18979.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Shares no sequence similarity with other isoforms due to a novel first exon containing the entire reading frame spliced to shared exon 2 so that exons 2-13 make up the 3'-UTR.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
PRO_0000203717

Regions

Nucleotide binding47 – 548GTP By similarity
Nucleotide binding198 – 2047GTP By similarity
Nucleotide binding223 – 2275GTP By similarity
Nucleotide binding292 – 2954GTP By similarity

Sites

Metal binding541Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site3661GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue3521Phosphoserine By similarity
Lipidation21N-palmitoyl glycine Ref.5
Lipidation31S-palmitoyl cysteine Ref.5
Cross-link300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence71 – 8414Missing in isoform Gnas-2.
VSP_001832

Experimental info

Sequence conflict181A → G in AAA30560. Ref.2
Sequence conflict851D → S in AAA30560. Ref.2
Sequence conflict3631F → S in AAA30560. Ref.2

Secondary structure

............................................................... 394
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gnas-1 (Alpha-S2) [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 4D07A734AFF2A6BC

FASTA39445,709
        10         20         30         40         50         60 
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM 

        70         80         90        100        110        120 
RILHVNGFNG EGGEEDPQAA RSNSDGEKAT KVQDIKNNLK EAIETIVAAM SNLVPPVELA 

       130        140        150        160        170        180 
NPENQFRVDY ILSVMNVPDF DFPPEFYEHA KALWEDEGVR ACYERSNEYQ LIDCAQYFLD 

       190        200        210        220        230        240 
KIDVIKQDDY VPSDQDLLRC RVLTSGIFET KFQVDKVNFH MFDVGGQRDE RRKWIQCFND 

       250        260        270        280        290        300 
VTAIIFVVAS SSYNMVIRED NQTNRLQEAL NLFKSIWNNR WLRTISVILF LNKQDLLAEK 

       310        320        330        340        350        360 
VLAGKSKIED YFPEFARYTT PEDATPEPGE DPRVTRAKYF IRDEFLRIST ASGDGRHYCY 

       370        380        390 
PHFTCAVDTE NIRRVFNDCR DIIQRMHLRQ YELL 

« Hide

Isoform Gnas-2 (Alpha-S1) [UniParc].

Checksum: 5B06C75B1A366920
Show »

FASTA38044,280
Isoform Nesp55 [UniParc].

See O18979.

References

« Hide 'large scale' references
[1]"Primary structure of the alpha-subunit of bovine adenylate cyclase-stimulating G-protein deduced from the cDNA sequence."
Nukada T., Tanabe T., Takahashi H., Noda M., Hirose T., Inayama S., Numa S.
FEBS Lett. 195:220-224(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Deduced primary structure of the alpha subunit of the GTP-binding stimulatory protein of adenylate cyclase."
Robishaw J.D., Russell D.W., Harris B.A., Smigel M.D., Gilman A.G.
Proc. Natl. Acad. Sci. U.S.A. 83:1251-1255(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus and Kidney.
[4]"Molecular basis for two forms of the G protein that stimulates adenylate cyclase."
Robishaw J.D., Smigel M.D., Gilman A.G.
J. Biol. Chem. 261:9587-9590(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
[5]"Galpha(s) is palmitoylated at the N-terminal glycine."
Kleuss C., Krause E.
EMBO J. 22:826-832(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT GLY-2 AND CYS-3, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Crystal structure of the adenylyl cyclase activator Gsalpha."
Sunahara R.K., Tesmer J.J.G., Gilman A.G., Sprang S.R.
Science 278:1943-1947(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-394 OF GNAS-2 FORM.
[7]"Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.
[8]"Two-metal-ion catalysis in adenylyl cyclase."
Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CATALYTIC DOMAINS OF ADENYLATE CYCLASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03404 mRNA. Translation: CAA27137.1.
M13006 mRNA. Translation: AAA30560.1.
BC102905 mRNA. Translation: AAI02906.1.
BC122757 mRNA. Translation: AAI22758.1.
M14014 mRNA. Translation: AAA30557.1.
PIRRGBOGA. A23818.
I45904.
RefSeqNP_001258700.1. NM_001271771.1.
NP_851364.1. NM_181021.3. [P04896-1]
UniGeneBt.64619.
Bt.91987.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZSX-ray2.30C1-394[»]
1AZTX-ray2.30A/B1-394[»]
1CJKX-ray3.00C1-394[»]
1CJTX-ray2.80C1-394[»]
1CJUX-ray2.80C1-394[»]
1CJVX-ray3.00C1-394[»]
1CS4X-ray2.50C1-394[»]
1CULX-ray2.40C1-394[»]
1TL7X-ray2.80C1-394[»]
1U0HX-ray2.90C1-394[»]
2GVDX-ray2.90C1-394[»]
2GVZX-ray3.27C1-394[»]
3C14X-ray2.68C1-394[»]
3C15X-ray2.78C1-394[»]
3C16X-ray2.87C1-394[»]
3G82X-ray3.11C1-394[»]
3MAAX-ray3.00C1-394[»]
3SN6X-ray3.20A1-394[»]
ProteinModelPortalP04896.
SMRP04896. Positions 35-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-588N.
IntActP04896. 1 interaction.
STRING9913.ENSBTAP00000023234.

Proteomic databases

PRIDEP04896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281793.
KEGGbta:281793.

Organism-specific databases

CTD2778.

Phylogenomic databases

eggNOGNOG325092.
HOGENOMHOG000038729.
HOVERGENHBG063184.
KOK04632.

Family and domain databases

Gene3D1.10.400.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR000367. Gprotein_alpha_S.
IPR001019. Gprotein_alpha_su.
IPR011025. GproteinA_insert.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR10218. PTHR10218. 1 hit.
PfamPF00503. G-alpha. 1 hit.
[Graphical view]
PRINTSPR00318. GPROTEINA.
PR00443. GPROTEINAS.
SMARTSM00275. G_alpha. 1 hit.
[Graphical view]
SUPFAMSSF47895. SSF47895. 1 hit.
SSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP04896.
NextBio20805706.

Entry information

Entry nameGNAS2_BOVIN
AccessionPrimary (citable) accession number: P04896
Secondary accession number(s): Q0II85, Q3SZE7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references